Reversible binding of modified biotinylated proteins on ultra-high-aspect-ratio nanostructures

ANYL 167

Jowell G. Bolivar1, Guofang Chen, gchen@lsu.edu2, Steven A. Soper, chsope@lsu.edu2, and Robin L. McCarley, tunnel@lsu.edu2. (1) Department of Chemistry, Louisiana State University, Baton Rouge, 306 Choppin Hall, Louisiana State University, Baton Rouge, LA 70803, (2) Department of Chemistry, Louisiana State University, 232 Choppin Hall, Baton Rouge, LA 70803
Described in this work is a methodology to reversibly bind biotinylated proteins on poly(methyl methacrylate), PMMA, microfluidic surfaces. The surfaces had tethered to them modified avidin (nitro-tyrosine in 42 position) capable of capturing biotinylated proteins, and the latter were readily released using high pH buffers. Surface plasmon resonance (SPR) experiments confirmed the binding propensity of the modified avidin for biotin, as noted by the ~ 10x change in binding constant. Quantitation of the nitrated sites in the modified avidin was also performed. In addition, ultra-high-aspect-ratio PMMA nanopillars were integrated into polymer-based microfluidic devices for high-efficiency capture of target analytes. Results from this study will be extended to the surface capture of phosphorylated proteins.

 

General Papers
7:00 PM-9:00 PM, Sunday, 28 August 2005 Washington DC Convention Center -- Hall A, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, 29 August 2005 Washington DC Convention Center -- Hall A, Sci-Mix

Division of Analytical Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005